TPM1 Human

Tropomyosin-1 Human Recombinant
Cat. No.
BT18914
Source
Escherichia Coli.
Synonyms
Tropomyosin alpha-1 chain, Tropomyosin-1, Alpha-tropomyosin, TPM1, C15orf13, TMSA, CMD1Y, HTM-alpha.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

TPM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 304 amino acids (1-284 a.a.) and having a total molecular mass of 35kDa (Molecular weight on SDS-PAGE will appear higher).
TPM1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Tropomyosin 1 (TPM1) belongs to the tropomyosin protein family, known for their highly conserved nature and widespread distribution. These proteins, with molecular weights ranging from 35 to 45 kDa, play crucial roles in the contractile systems of both striated and smooth muscles, as well as in the cytoskeleton of non-muscle cells. TPM1 itself is a dimer composed of two alpha-helical chains forming a coiled-coil structure. This protein polymerizes along the actin filaments, specifically within the grooves, contributing to filament stability. Its interaction with actin is observed in both muscle and non-muscle cells. In muscle cells, TPM1 collaborates with the troponin complex to regulate the calcium-dependent interaction between actin and myosin, essential for muscle contraction. Conversely, in non-muscle cells, TPM1 participates in stabilizing cytoskeleton actin filaments. Notably, in smooth muscle cells, the interaction between TPM1 and caldesmon governs smooth muscle contraction. Several alternatively spliced transcript variants of TPM1 exist, encoding a variety of isoforms with distinct expression patterns. For instance, Isoform 1 is found in both adult and fetal skeletal and cardiac muscles, exhibiting higher expression in cardiac tissues. On the other hand, Isoform 10 is specifically expressed in adult and fetal cardiac tissues, absent in skeletal muscle. Mutations in the TPM1 gene are implicated in the development of type 3 familial hypertrophic cardiomyopathy.
Description
Recombinant human TPM1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 304 amino acids, with a sequence spanning from amino acid positions 1 to 284, resulting in a molecular mass of 35 kDa. However, it's important to note that the apparent molecular weight on SDS-PAGE may be higher. The recombinant TPM1 protein is engineered with a 20 amino acid His Tag fused to its N-terminus. Purification is achieved through proprietary chromatographic methods.
Physical Appearance
The product is a clear solution that has been sterilized by filtration.
Formulation
The TPM1 protein solution has a concentration of 0.5 mg/ml and is supplied in a buffer consisting of 20 mM Tris-HCl (pH 8), 1 mM DTT, 0.1 M NaCl, and 20% glycerol.
Stability
For short-term storage (up to 4 weeks), the unopened vial should be kept refrigerated at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein such as HSA or BSA (0.1%) is advisable. Repeated freeze-thaw cycles should be minimized.
Purity
The purity of the TPM1 protein is determined by SDS-PAGE analysis and is consistently greater than 90.0%.
Synonyms
Tropomyosin alpha-1 chain, Tropomyosin-1, Alpha-tropomyosin, TPM1, C15orf13, TMSA, CMD1Y, HTM-alpha.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY SEALKDAQEK
LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR
KYEEVARKLV IIESDLERAE ERAELSEGQV RQLEEQLRIM DQTLKALMAA EDKYSQKEDR YEEEIKVLSD KLKEAETRAE FAERSVTKLE
KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSM.

Product Science Overview

Introduction

Tropomyosin-1 (TPM1) is a member of the tropomyosin family, which consists of highly conserved, widely distributed actin-binding proteins. These proteins play a crucial role in the contractile system of striated and smooth muscles, as well as in the cytoskeleton of non-muscle cells .

Structure and Function

Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It polymerizes end-to-end along the two grooves of actin filaments, providing stability to the filaments . TPM1 is one type of alpha-helical chain that forms the predominant tropomyosin of striated muscle. It functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction .

Recombinant Human Tropomyosin-1

Recombinant human TPM1 protein is typically fused to a His-tag at the N-terminus and expressed in E. coli. The protein is then purified using conventional chromatography techniques . The recombinant protein has a theoretical molecular weight of approximately 35 kDa, although the observed molecular weight may vary due to post-translational modifications and other experimental factors .

Applications

Recombinant human TPM1 is used in various research applications, including studies on muscle contraction, cytoskeletal dynamics, and genetic regulation of hematopoiesis . For instance, CRISPR/Cas9-mediated TPM1 knockout in human induced pluripotent stem cells (iPSCs) has been shown to enhance hematopoietic progenitor development, increasing total megakaryocyte and erythroid cell yields .

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